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Protein

Protein AF1q

Gene

MLLT11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cofactor for the transcription factor TCF7 (PubMed:26079538). Involved in regulation of lymphoid development by driving multipotent hematopoietic progenitor cells towards a T cell fate (PubMed:21715312).2 Publications

GO - Biological processi

  • extrinsic apoptotic signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of mitochondrial depolarization Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AF1q
Gene namesi
Name:MLLT11
Synonyms:AF1Q
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:16997. MLLT11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • intracellular Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MLLT11 is found in acute leukemias. Translocation t(1;11)(q21;q23) with KMT2A/MLL1.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 329LSELEGLGL → ASEAEGAGA: Constitutive nuclear sequestration. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA142671347.

Polymorphism and mutation databases

BioMutaiMLLT11.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9090Protein AF1qPRO_0000064471Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated, leading to degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13015.
PaxDbiQ13015.
PeptideAtlasiQ13015.
PRIDEiQ13015.
TopDownProteomicsiQ13015.

PTM databases

iPTMnetiQ13015.
PhosphoSiteiQ13015.

Expressioni

Tissue specificityi

Expressed in myoepithelial cells of normal breast tissue (at protein level) (PubMed:26079538). Highly expressed in thymus (PubMed:7833468). Expressed in colon, small intestine, prostate and ovary. Not detected in peripheral blood lymphocytes and spleen (PubMed:7833468).2 Publications

Gene expression databases

BgeeiQ13015.
CleanExiHS_MLLT11.
ExpressionAtlasiQ13015. baseline and differential.
GenevisibleiQ13015. HS.

Organism-specific databases

HPAiHPA000540.

Interactioni

Subunit structurei

Interacts with HSPA8 and LAMP2 isoform A; the interaction may target MLLT11 for degradation via chaperone-mediated autophagy (PubMed:24880125). Interacts with TCF7 (PubMed:26079538).2 Publications

Protein-protein interaction databases

BioGridi116161. 4 interactions.
IntActiQ13015. 3 interactions.
MINTiMINT-4718428.
STRINGi9606.ENSP00000357917.

Structurei

3D structure databases

ProteinModelPortaliQ13015.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi24 – 329Nuclear export signal1 Publication

Sequence similaritiesi

Belongs to the MLLT11 family.Curated

Phylogenomic databases

eggNOGiENOG410IZF7. Eukaryota.
ENOG4112CHF. LUCA.
HOGENOMiHOG000033833.
InParanoidiQ13015.
OMAiKMTGQAT.
OrthoDBiEOG7TBC4V.
PhylomeDBiQ13015.
TreeFamiTF336906.

Family and domain databases

InterProiIPR026778. MLLT11_fam.
IPR033461. WRNPLPNID.
[Graphical view]
PANTHERiPTHR15404. PTHR15404. 1 hit.
PfamiPF15017. WRNPLPNID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRDPVSSQYS SFLFWRMPIP ELDLSELEGL GLSDTATYKV KDSSVGKMIG
60 70 80 90
QATAADQEKN PEGDGLLEYS TFNFWRAPIA SIHSFELDLL
Length:90
Mass (Da):10,061
Last modified:November 1, 1996 - v1
Checksum:iB37C6F7303C9EBF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16954 mRNA. Translation: AAA70088.1.
BT006799 mRNA. Translation: AAP35445.1.
CR456879 mRNA. Translation: CAG33160.1.
AL590133 Genomic DNA. Translation: CAI13350.1.
BC006471 mRNA. No translation available.
BC008445 mRNA. Translation: AAH08445.1.
BC009624 mRNA. Translation: AAH09624.1.
BC019253 mRNA. Translation: AAH19253.1.
BC021703 mRNA. Translation: AAH21703.1.
BC022448 mRNA. Translation: AAH22448.1.
CCDSiCCDS982.1.
PIRiI38889.
RefSeqiNP_006809.1. NM_006818.3.
UniGeneiHs.75823.

Genome annotation databases

EnsembliENST00000368921; ENSP00000357917; ENSG00000213190.
GeneIDi10962.
KEGGihsa:10962.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16954 mRNA. Translation: AAA70088.1.
BT006799 mRNA. Translation: AAP35445.1.
CR456879 mRNA. Translation: CAG33160.1.
AL590133 Genomic DNA. Translation: CAI13350.1.
BC006471 mRNA. No translation available.
BC008445 mRNA. Translation: AAH08445.1.
BC009624 mRNA. Translation: AAH09624.1.
BC019253 mRNA. Translation: AAH19253.1.
BC021703 mRNA. Translation: AAH21703.1.
BC022448 mRNA. Translation: AAH22448.1.
CCDSiCCDS982.1.
PIRiI38889.
RefSeqiNP_006809.1. NM_006818.3.
UniGeneiHs.75823.

3D structure databases

ProteinModelPortaliQ13015.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116161. 4 interactions.
IntActiQ13015. 3 interactions.
MINTiMINT-4718428.
STRINGi9606.ENSP00000357917.

PTM databases

iPTMnetiQ13015.
PhosphoSiteiQ13015.

Polymorphism and mutation databases

BioMutaiMLLT11.

Proteomic databases

EPDiQ13015.
PaxDbiQ13015.
PeptideAtlasiQ13015.
PRIDEiQ13015.
TopDownProteomicsiQ13015.

Protocols and materials databases

DNASUi10962.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368921; ENSP00000357917; ENSG00000213190.
GeneIDi10962.
KEGGihsa:10962.

Organism-specific databases

CTDi10962.
GeneCardsiMLLT11.
HGNCiHGNC:16997. MLLT11.
HPAiHPA000540.
MIMi604684. gene.
neXtProtiNX_Q13015.
PharmGKBiPA142671347.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZF7. Eukaryota.
ENOG4112CHF. LUCA.
HOGENOMiHOG000033833.
InParanoidiQ13015.
OMAiKMTGQAT.
OrthoDBiEOG7TBC4V.
PhylomeDBiQ13015.
TreeFamiTF336906.

Miscellaneous databases

ChiTaRSiMLLT11. human.
GenomeRNAii10962.
PROiQ13015.
SOURCEiSearch...

Gene expression databases

BgeeiQ13015.
CleanExiHS_MLLT11.
ExpressionAtlasiQ13015. baseline and differential.
GenevisibleiQ13015. HS.

Family and domain databases

InterProiIPR026778. MLLT11_fam.
IPR033461. WRNPLPNID.
[Graphical view]
PANTHERiPTHR15404. PTHR15404. 1 hit.
PfamiPF15017. WRNPLPNID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene, AF1q, fused to MLL in t(1;11)(q21;q23), is specifically expressed in leukemic and immature hematopoietic cells."
    Tse W., Zhu W., Chen H.S., Cohen A.
    Blood 85:650-656(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL REARRANGEMENT, TISSUE SPECIFICITY.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow, Brain and Lung.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "AF1q/MLLT11 regulates the emergence of human prothymocytes through cooperative interaction with the Notch signaling pathway."
    Parcelier A., Maharzi N., Delord M., Robledo-Sarmiento M., Nelson E., Belakhdar-Mekid H., Pla M., Kuranda K., Parietti V., Goodhardt M., Legrand N., Bernstein I.D., Gluckman J.C., Sigaux F., Canque B.
    Blood 118:1784-1796(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 24-LEU--LEU-32, UBIQUITINATION, NUCLEAR EXPORT SIGNAL.
  8. "Degradation of AF1Q by chaperone-mediated autophagy."
    Li P., Ji M., Lu F., Zhang J., Li H., Cui T., Li Wang X., Tang D., Ji C.
    Exp. Cell Res. 327:48-56(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPA8 AND LAMP2.
  9. "AF1q is a novel TCF7 co-factor which activates CD44 and promotes breast cancer metastasis."
    Park J., Schlederer M., Schreiber M., Ice R., Merkel O., Bilban M., Hofbauer S., Kim S., Addison J., Zou J., Ji C., Bunting S.T., Wang Z., Shoham M., Huang G., Bago-Horvath Z., Gibson L.F., Rojanasakul Y.
    , Remick S., Ivanov A., Pugacheva E., Bunting K.D., Moriggl R., Kenner L., Tse W.
    Oncotarget 6:20697-20710(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TCF7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAF1Q_HUMAN
AccessioniPrimary (citable) accession number: Q13015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.